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      The rice immune receptor XA21 recognizes a tyrosine-sulfated protein from a Gram-negative bacterium

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      1 , 2 , 1 , 2 , 3 , , 1 , 2 , 1 , 1 , 4 , 5 , 2 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 6 , 2 , 1 , 2 , 1 , 1 , 2 , 7 , 8 , 8 , 9 , 2 , 6 , 10 , 5 , 4 , 1 , 2 ,
      Science Advances
      American Association for the Advancement of Science
      Rice, immune receptors, Bacteria

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          Abstract

          A sulfated peptide activates a rice immune receptor.

          Abstract

          Surveillance of the extracellular environment by immune receptors is of central importance to eukaryotic survival. The rice receptor kinase XA21, which confers robust resistance to most strains of the Gram-negative bacterium Xanthomonas oryzae pv. oryzae ( Xoo), is representative of a large class of cell surface immune receptors in plants and animals. We report the identification of a previously undescribed Xoo protein, called RaxX, which is required for activation of XA21-mediated immunity. Xoo strains that lack RaxX, or carry mutations in the single RaxX tyrosine residue (Y41), are able to evade XA21-mediated immunity. Y41 of RaxX is sulfated by the prokaryotic tyrosine sulfotransferase RaxST. Sulfated, but not nonsulfated, RaxX triggers hallmarks of the plant immune response in an XA21-dependent manner. A sulfated, 21–amino acid synthetic RaxX peptide (RaxX21-sY) is sufficient for this activity. Xoo field isolates that overcome XA21-mediated immunity encode an alternate raxX allele, suggesting that coevolutionary interactions between host and pathogen contribute to RaxX diversification. RaxX is highly conserved in many plant pathogenic Xanthomonas species. The new insights gained from the discovery and characterization of the sulfated protein, RaxX, can be applied to the development of resistant crop varieties and therapeutic reagents that have the potential to block microbial infection of both plants and animals.

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          Most cited references44

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          Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation.

          Higher eukaryotes sense microbes through the perception of pathogen-associated molecular patterns (PAMPs). Arabidopsis plants detect a variety of PAMPs including conserved domains of bacterial flagellin and of bacterial EF-Tu. Here, we show that flagellin and EF-Tu activate a common set of signaling events and defense responses but without clear synergistic effects. Treatment with either PAMP results in increased binding sites for both PAMPs. We used this finding in a targeted reverse-genetic approach to identify a receptor kinase essential for EF-Tu perception, which we called EFR. Nicotiana benthamiana, a plant unable to perceive EF-Tu, acquires EF-Tu binding sites and responsiveness upon transient expression of EFR. Arabidopsis efr mutants show enhanced susceptibility to the bacterium Agrobacterium tumefaciens, as revealed by a higher efficiency of T-DNA transformation. These results demonstrate that EFR is the EF-Tu receptor and that plant defense responses induced by PAMPs such as EF-Tu reduce transformation by Agrobacterium.
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            Plant PRRs and the activation of innate immune signaling.

            Despite being sessile organisms constantly exposed to potential pathogens and pests, plants are surprisingly resilient to infections. Plants can detect invaders via the recognition of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs). Plant PRRs are surface-localized receptor-like kinases, which comprise a ligand-binding ectodomain and an intracellular kinase domain, or receptor-like proteins, which do not exhibit any known intracellular signaling domain. In this review, we summarize recent discoveries that shed light on the molecular mechanisms underlying ligand perception and subsequent activation of plant PRRs. Notably, plant PRRs appear as central components of multiprotein complexes at the plasma membrane that contain additional transmembrane and cytosolic kinases required for the initiation and specificity of immune signaling. PRR complexes are under tight control by protein phosphatases, E3 ligases, and other regulatory proteins, illustrating the exquisite and complex regulation of these molecular machines whose proper activation underlines a crucial layer of plant immunity. Copyright © 2014 Elsevier Inc. All rights reserved.
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              A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21.

              The rice Xa21 gene, which confers resistance to Xanthomonas oryzae pv. oryzae race 6, was isolated by positional cloning. Fifty transgenic rice plants carrying the cloned Xa21 gene display high levels of resistance to the pathogen. The sequence of the predicted protein, which carries both a leucine-rich repeat motif and a serine-threonine kinase-like domain, suggests a role in cell surface recognition of a pathogen ligand and subsequent activation of an intracellular defense response. Characterization of Xa21 should facilitate understanding of plant disease resistance and lead to engineered resistance in rice.
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                Author and article information

                Journal
                Sci Adv
                Sci Adv
                SciAdv
                advances
                Science Advances
                American Association for the Advancement of Science
                2375-2548
                July 2015
                24 July 2015
                : 1
                : 6
                : e1500245
                Affiliations
                [1 ]Department of Plant Pathology and the Genome Center, University of California, Davis, Davis, CA 95616, USA.
                [2 ]Joint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
                [3 ]The Australian National University, Research School of Biology, Acton ACT 2601, Australia.
                [4 ]Centre for Plant Molecular Biology, University of Tübingen, 72074 Tübingen, Germany.
                [5 ]Department of Chemistry, University of Texas at Austin, Austin, TX 78712, USA.
                [6 ]Department of Biomedical Engineering, University of California, Irvine, Irvine, CA 92697, USA.
                [7 ]Interfaculty Institute of Biochemistry, University of Tübingen, 72074 Tübingen, Germany.
                [8 ]Council of Scientific & Industrial Research (CSIR)–Institute of Microbial Technology, Chandigarh 160036, India.
                [9 ]CSIR–Centre for Cellular and Molecular Biology, Hyderabad 500007, India.
                [10 ]Department of Chemistry, University of California, Irvine, Irvine, CA 92697, USA.
                Author notes
                [*]

                These authors contributed equally to this work.

                []Corresponding author. E-mail: benjamin.schwessinger@ 123456anu.edu.au (B.S.); pcronald@ 123456ucdavis.edu (P.C.R.)
                Article
                1500245
                10.1126/sciadv.1500245
                4646787
                26601222
                4a1e166d-8fdd-4581-bc54-18eb47f2a1b5
                Copyright © 2015, The Authors

                This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license, which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.

                History
                : 02 March 2015
                : 14 May 2015
                Funding
                Funded by: National Institutes of Health;
                Award ID: ID0EEXBG1386
                Award ID: NIH GM59962
                Award Recipient :
                Funded by: U.S. Department of Energy;
                Award ID: ID0EZ2BG1387
                Award ID: DE-AC02-05CH11231
                Award Recipient :
                Funded by: European Molecular Biology Organization;
                Award ID: ID0EPAAI1388
                Award ID: ALTF 1290-2011
                Award Recipient :
                Funded by: Human Frontier Science Program;
                Award ID: ID0EHCAI1389
                Award ID: LT000674/2012
                Award Recipient :
                Funded by: Council of Scientific and Industrial Research;
                Award ID: ID0E6DAI1390
                Award ID: BSC0117
                Award Recipient :
                Funded by: National Institutes of Health;
                Award ID: ID0EVFAI1391
                Award ID: GM099028
                Award Recipient :
                Funded by: Welch Foundation;
                Award ID: ID0ELHAI1392
                Award ID: F1155
                Award Recipient :
                Categories
                Research Article
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                Crop Science
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                Michael Sabado

                rice,immune receptors,bacteria
                rice, immune receptors, bacteria

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